Development of a highly potent, selective, and cell-active inhibitor of cysteine cathepsin L-A hybrid design approach

Chem Commun (Camb). 2014 Sep 25;50(74):10875-8. doi: 10.1039/c4cc04037f. Epub 2014 Aug 4.

Abstract

A hybrid-design approach is undertaken to develop a highly potent and selective inhibitor of human cathepsin L. Studies involving human breast carcinoma MDA-MB-231 cells establish that this inhibitor can successfully block intracellular cathepsin L activity, and retard the cell-migratory potential of these highly metastatic cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cathepsin L / antagonists & inhibitors*
  • Cathepsin L / metabolism
  • Cell Line, Tumor
  • Cell Movement / drug effects
  • Collagen Type I / metabolism
  • Cysteine Proteinase Inhibitors / chemistry
  • Cysteine Proteinase Inhibitors / metabolism
  • Cysteine Proteinase Inhibitors / pharmacology
  • Drug Design
  • Humans
  • Kinetics
  • Protein Binding

Substances

  • Collagen Type I
  • Cysteine Proteinase Inhibitors
  • Cathepsin L